ID W9XFI9_9EURO Unreviewed; 932 AA.
AC W9XFI9;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 13-SEP-2023, entry version 39.
DE RecName: Full=Rho-GAP domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=A1O3_08478 {ECO:0000313|EMBL:EXJ78978.1};
OS Capronia epimyces CBS 606.96.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Capronia.
OX NCBI_TaxID=1182542 {ECO:0000313|EMBL:EXJ78978.1, ECO:0000313|Proteomes:UP000019478};
RN [1] {ECO:0000313|EMBL:EXJ78978.1, ECO:0000313|Proteomes:UP000019478}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 606.96 {ECO:0000313|EMBL:EXJ78978.1,
RC ECO:0000313|Proteomes:UP000019478};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Capronia epimyces CBS 606.96.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EXJ78978.1}.
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DR EMBL; AMGY01000008; EXJ78978.1; -; Genomic_DNA.
DR RefSeq; XP_007736766.1; XM_007738576.1.
DR AlphaFoldDB; W9XFI9; -.
DR STRING; 1182542.W9XFI9; -.
DR GeneID; 19172566; -.
DR eggNOG; ENOG502QQWB; Eukaryota.
DR HOGENOM; CLU_008201_1_0_1; -.
DR OrthoDB; 1328399at2759; -.
DR Proteomes; UP000019478; Unassembled WGS sequence.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProt.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR CDD; cd04399; RhoGAP_fRGD2; 1.
DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 2.
DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR000591; DEP_dom.
DR InterPro; IPR031160; F_BAR.
DR InterPro; IPR001060; FCH_dom.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR23065; PROLINE-SERINE-THREONINE PHOSPHATASE INTERACTING PROTEIN 1; 1.
DR PANTHER; PTHR23065:SF17; RHO-GTPASE-ACTIVATING PROTEIN RGD2; 1.
DR Pfam; PF00610; DEP; 1.
DR Pfam; PF00611; FCH; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00055; FCH; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS50186; DEP; 1.
DR PROSITE; PS51741; F_BAR; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|PROSITE-ProRule:PRU01077};
KW Reference proteome {ECO:0000313|Proteomes:UP000019478}.
FT DOMAIN 14..445
FT /note="F-BAR"
FT /evidence="ECO:0000259|PROSITE:PS51741"
FT DOMAIN 242..310
FT /note="DEP"
FT /evidence="ECO:0000259|PROSITE:PS50186"
FT DOMAIN 479..686
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 695..932
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 695..716
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 717..752
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 794..825
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 839..853
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 898..921
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 932 AA; 103070 MW; B08D7B2C1B7B1B96 CRC64;
MANESIPSPR PKVPGFTDAF WSTDYAGGLG VLFQKLQQGV IENQQVLTIA SMRADAEEMY
SDQLGDIAPT IDRMTGGFSR DDGASVRKAY EGVRSEMIEA SKNHRKIADN IRELVVHPFS
RWCDAHATRI QNSQDDLQAK IKAHDRQAEV VKKLRSHYFN KCRLVEDLEE ENKLAFQAPG
KESPKAQSPP PPRIVLPEDD AEELPVEIGD ETYPPQQLKA LLTHMLETIP LGEYKVPILG
LYQNVSAGTD IVDYIQKHMK ASTVGYAEKI GQDLVDRGFL RLIGNVGNTF ANSSRMKYQW
KSRVFQITGV PEKKKPLGRS ATGSSMEGLL ESPTIGNITE TLQTWNPLNN PHPNETPAER
LRREAREADE KYKAAVRKLD LLRCHLEESM MDHLKFLERC ETDRLRAIKA VILDFSGAIS
NSIPSFQSQV DHMMLYQETI QPLGDLRYLL ENYKTGAYVP KVTPYENYYG TVVDQTFGVD
LEARARADRK RVPIVVTSIL TFLDNHYPDL EGDEARRNIW LLDVPLAATH HLRNQINNGA
PVSPEILEKY EVPIVASVLK LYLLELPDSL VSAQVYEIIK TIYATTPDAV PNPISSDSID
ATPRIKVLQS TLGQLRLNNI ATLDAIVTHF ARLIDLTSAD DAYVTTLAQS LAPCILRPRI
ENSLTLEERH PYRLVRDLFD YKEAIFGELK RQSSTRTVSE SISHRQRAVS NTDESSRRAA
MEARAKAITE QRQRDKSPAP SSRHRRDKST DGSLGRFPVV ASPRLDHGRS VSAAGLPSAK
RSSLEVPGSV EGSPVQARNL SATERNSATK IEVSGTTTNG QGEPSPSILH LPGTFSGGGP
GPHIPPPPED DSQEEQSPAP APAAREPGQE QTPRVGSLKR SGAATERKPV GRSGPGSLSR
RINPSGMDET SPATIATPQG VQLTDKPMDD FA
//
